page_title: Alpha-D-phosphohexomutase superfamily
section_title: Structure and oligomeric state
hierarchical_section_title: Alpha-D-phosphohexomutase superfamily / Structure and oligomeric state
caption_attribution_description: English: A superposition of four enzymes from the alpha D phosphohexomutase superfamily, one from each subgroup, demonstrating the structural similarity of all members in the superfamily.
context_page_description: The alpha-D-phosphohexomutases are a large superfamily of enzymes, with members in all three domains of life. Enzymes from this superfamily are ubiquitous in organisms from E. Coli to humans, and catalyze a phosphoryl transfer reaction on a phosphosugar substrate. Four well studied subgroups in the superfamily are:
  Phosphoglucomutase
  Phosphoglucomutase/Phosphomannomutase
  Phosphoglucosamine mutase
  Phosphoaceytlglucosamine mutase
  Other enzymes in the superfamily are known to act as glucose 1,6-bisphosphate synthases and phosphopentomutases.
context_section_description: Structures of multiple enzymes have been determined through X-ray crystallography. In general, they share a very similar topology. With a heart-shape and four domains (see image below), most enzymes appear to be monomers.
  However some are known to exist as dimers or tetramers in solution. Eleven crystal structures for this superfamily have been determined thus far, six of which are likely oligomers. Two distinct dimers and one tetrameric arrangement has been documented.
caption: A superposition of four enzymes from the alpha D phosphohexomutase superfamily, one from each subgroup, demonstrating the structural similarity of all members in the superfamily.
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